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Conserved domains on  [gi|1485816994|gb|AYE91700|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Cardiodactylus enkraussi]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 999987)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

CATH:  1.10.287.90
EC:  7.1.1.9
Gene Ontology:  GO:0004129|GO:0005507
PubMed:  6307356|8083153
TCDB:  3.D.4.6.2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 super family cl33359
cytochrome c oxidase subunit II; Provisional
 3-110 3.75e-51

cytochrome c oxidase subunit II; Provisional


The actual alignment was detected with superfamily member MTH00154:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 160.76  E-value: 3.75e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDLYFKNHVEFDSYMV--LPETLSSFRLLDVDNH 80
Cdd:MTH00154   62 EIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNR 141

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00154  142 LVLPMNTQIRILITAADVIHSWTVPSLGVK 171
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 3-110 3.75e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 160.76  E-value: 3.75e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDLYFKNHVEFDSYMV--LPETLSSFRLLDVDNH 80
Cdd:MTH00154   62 EIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNR 141

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00154  142 LVLPMNTQIRILITAADVIHSWTVPSLGVK 171
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 34-110 8.73e-36

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 118.44  E-value: 8.73e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1485816994  34 PMITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLS--SFRLLDVDNHTMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEkgQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
36-110 1.83e-30

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 104.80  E-value: 1.83e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1485816994  36 ITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLS--SFRLLDVDNHTMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEegQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIK 77
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-110 7.23e-13

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 61.77  E-value: 7.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDlYFKNHVEFDSYMVLPEtlssfrlldvdnhtm 82
Cdd:COG1622    80 EIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFR-YPDQGIATVNELVLPV--------------- 143

                          90       100
                  ....*....|....*....|....*...
gi 1485816994  83 lpmNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:COG1622   144 ---GRPVRFLLTSADVIHSFWVPALGGK 168
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-110 1.29e-09

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 52.77  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   2 SESIWTILPAIVLIFIALPSLRLLYLLDESMNP-MITLKTIGHQWYCSYDLyfknhvefdsymvlPETLSSfrlldVDNH 80
Cdd:TIGR02866  56 LEYVWTVIPLIIVVGLFAATAKGLLYLERPIPKdALKVKVTGYQWWWDFEY--------------PESGFT-----TVNE 116

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:TIGR02866 117 LVLPAGTPVELQVTSKDVIHSFWVPELGGK 146
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 3-110 3.75e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 160.76  E-value: 3.75e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDLYFKNHVEFDSYMV--LPETLSSFRLLDVDNH 80
Cdd:MTH00154   62 EIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNR 141

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00154  142 LVLPMNTQIRILITAADVIHSWTVPSLGVK 171
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 3-110 2.66e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 135.62  E-value: 2.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLSS--FRLLDVDNH 80
Cdd:MTH00139   62 ETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSgeFRLLEVDNR 141

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00139  142 LVLPYKSNIRALITAADVLHSWTVPSLGVK 171
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 3-110 4.75e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 135.04  E-value: 4.75e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLS--SFRLLDVDNH 80
Cdd:MTH00117   62 ELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPngHFRLLEVDHR 141

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00117  142 MVIPMESPIRILITAEDVLHSWAVPSLGVK 171
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 3-110 2.05e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 133.53  E-value: 2.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLSS--FRLLDVDNH 80
Cdd:MTH00140   62 ETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELgdFRLLEVDNR 141

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00140  142 LVLPYSVDTRVLVTSADVIHSWTVPSLGVK 171
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-110 6.74e-40

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 132.29  E-value: 6.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   1 TSESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLS--SFRLLDVD 78
Cdd:MTH00008   60 QIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSpgQFRLLEVD 139

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1485816994  79 NHTMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00008  140 NRAVLPMQTEIRVLVTAADVIHSWTVPSLGVK 171
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 3-110 1.85e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 130.98  E-value: 1.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLSS--FRLLDVDNH 80
Cdd:MTH00038   62 ETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTglPRLLEVDNR 141

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00038  142 LVLPYQTPIRVLVSSADVLHSWAVPSLGVK 171
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 3-110 2.22e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 128.17  E-value: 2.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLS--SFRLLDVDNH 80
Cdd:MTH00168   62 EFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSpgQFRLLEVDNR 141

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00168  142 LVLPMDSKIRVLVTSADVLHSWTLPSLGLK 171
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 3-110 2.59e-36

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 123.32  E-value: 2.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDL--YFKNHVEFDSYMVLPETLSS--FRLLDVD 78
Cdd:MTH00023   71 EIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYsdYEGETLEFDSYMVPTSDLNSgdFRLLEVD 150

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1485816994  79 NHTMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00023  151 NRLVVPINTHVRILVTGADVLHSFAVPSLGLK 182
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 34-110 8.73e-36

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 118.44  E-value: 8.73e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1485816994  34 PMITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLS--SFRLLDVDNHTMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEkgQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 3-110 2.06e-35

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 120.59  E-value: 2.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLS--SFRLLDVDNH 80
Cdd:MTH00098   62 ETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKpgELRLLEVDNR 141

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00098  142 VVLPMEMPIRMLISSEDVLHSWAVPSLGLK 171
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 3-110 5.11e-34

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 117.19  E-value: 5.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDL--YFKNHVEFDSYMVLPETLSS--FRLLDVD 78
Cdd:MTH00051   64 EIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYsdYGTDTIEFDSYMIPTSDLNSgdLRLLEVD 143

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1485816994  79 NHTMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00051  144 NRLIVPIQTQVRVLVTAADVLHSFAVPSLSVK 175
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 3-110 2.19e-33

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 115.26  E-value: 2.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLS--SFRLLDVDNH 80
Cdd:MTH00076   62 EMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTpgQFRLLEVDNR 141

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00076  142 MVVPMESPIRMLITAEDVLHSWAVPSLGIK 171
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 3-110 1.83e-32

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 113.27  E-value: 1.83e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLS--SFRLLDVDNH 80
Cdd:MTH00129   62 EIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTpgQFRLLEADHR 141

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00129  142 MVVPVESPIRVLVSAEDVLHSWAVPALGVK 171
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 3-110 2.69e-32

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 112.67  E-value: 2.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLSS--FRLLDVDNH 80
Cdd:MTH00185   62 EIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPgqFRLLETDHR 141

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00185  142 MVVPMESPIRVLITAEDVLHSWTVPALGVK 171
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
36-110 1.83e-30

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 104.80  E-value: 1.83e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1485816994  36 ITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLS--SFRLLDVDNHTMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEegQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIK 77
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 3-110 1.29e-25

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 96.25  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDES-MNPMITLKTIGHQWYCSYDL--YFKNHVEFDSYMVLPETLS--SFRLLDV 77
Cdd:MTH00027   93 EVIWTLIPAFILILIAFPSLRLLYIMDECgFSANITIKVTGHQWYWSYSYedYGEKNIEFDSYMIPTADLEfgDLRLLEV 172

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1485816994  78 DNHTMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00027  173 DNRLILPVDTNVRVLITAADVLHSWTVPSLAVK 205
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 3-110 8.36e-25

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 93.54  E-value: 8.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLdESMN--PMITLKTIGHQWYCSYDLYFKNHVEFDSYMVLPETLS--SFRLLDVD 78
Cdd:MTH00080   64 ELLCSVFPVLILLMQMVPSLSLLYYY-GLMNldSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRlgEPRLLEVD 142

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1485816994  79 NHTMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00080  143 NRCVLPCDTNIRFCITSSDVIHSWALPSLSIK 174
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-110 7.23e-13

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 61.77  E-value: 7.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPAIVLIFIALPSLRLLYLLDESMNPMITLKTIGHQWYCSYDlYFKNHVEFDSYMVLPEtlssfrlldvdnhtm 82
Cdd:COG1622    80 EIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFR-YPDQGIATVNELVLPV--------------- 143

                          90       100
                  ....*....|....*....|....*...
gi 1485816994  83 lpmNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:COG1622   144 ---GRPVRFLLTSADVIHSFWVPALGGK 168
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 59-110 9.15e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 60.60  E-value: 9.15e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1485816994  59 FDSYMVLPETLSS--FRLLDVDNHTMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:PTZ00047   51 FQSNLVTDEDLKPgmLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIK 104
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 3-110 1.65e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 60.35  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   3 ESIWTILPA-IVLIFIALPSLRLLYLLDESMNPMItlKTIGHQWYCSYDLyfKNHVEFDSYMvlpetlSSFRLLdVDNHT 81
Cdd:MTH00047   50 ELLWTVVPTlLVLVLCFLNLNFITSDLDCFSSETI--KVIGHQWYWSYEY--SFGGSYDSFM------TDDIFG-VDKPL 118

                          90       100
                  ....*....|....*....|....*....
gi 1485816994  82 MLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:MTH00047  119 RLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-110 1.29e-09

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 52.77  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485816994   2 SESIWTILPAIVLIFIALPSLRLLYLLDESMNP-MITLKTIGHQWYCSYDLyfknhvefdsymvlPETLSSfrlldVDNH 80
Cdd:TIGR02866  56 LEYVWTVIPLIIVVGLFAATAKGLLYLERPIPKdALKVKVTGYQWWWDFEY--------------PESGFT-----TVNE 116

                          90       100       110
                  ....*....|....*....|....*....|
gi 1485816994  81 TMLPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:TIGR02866 117 LVLPAGTPVELQVTSKDVIHSFWVPELGGK 146
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 36-110 3.36e-04

Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 36.89  E-value: 3.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485816994  36 ITLKTIGHQWYCSYdlYFKNHVEFDSYMVlpetlssfrlldvdnhtmlPMNTQIRTLVTAADVIHSWTIPTLGMK 110
Cdd:cd13842     1 LTVYVTGVQWSWTF--IYPNVRTPNEIVV-------------------PAGTPVRFRVTSPDVIHGFYIPNLGVK 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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